Anti-glycopeptide mAb LpMab-21 against Podoplanin
Kaneko, Mika K. Tohoku University
Nakamura, Takuro Tohoku University
Honma, Ryusuke Tohoku University|Yamagata University
Ogasawara, Satoshi Tohoku University
Fujii, Yuki Tohoku University
Abe, Shinji Tokushima University Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Takagi, Michiaki Yamagata University
Harada, Hiroyuki Tokyo Medical and Dental University
Suzuki, Hiroyoshi Sendai Medical Center
Nishioka, Yasuhiko Tokushima University Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Kato, Yukinari Tohoku University
Human podoplanin (hPDPN), which binds to C‐type lectin‐like receptor‐2 (CLEC‐2), is involved in platelet aggregation and cancer metastasis. The expression of hPDPN in cancer cells or cancer‐associated fibroblasts indicates poor prognosis. Human lymphatic endothelial cells, lung‐type I alveolar cells, and renal glomerular epithelial cells express hPDPN. Although numerous monoclonal antibodies (mA bs) against hPDPN are available, they recognize peptide epitopes of hPDPN. Here, we generated a novel anti‐hPDPN mA b, LpMab‐21. To characterize the hPDPN epitope recognized by the LpMab‐21, we established glycan‐deficient CHO‐S and HEK‐293T cell lines, using the CRISPR/Cas9 or TALEN. Flow cytometric analysis revealed that the minimum hPDPN epitope, in which sialic acid is linked to Thr76, recognized by LpMab‐21 is Thr76–Arg79. LpMab‐21 detected hPDPN expression in glioblastoma, oral squamous carcinoma, and seminoma cells as well as in normal lymphatic endothelial cells. However, LpMab‐21 did not react with renal glomerular epithelial cells or lung type I alveolar cells, indicating that sialylation of hPDPN Thr76 is cell‐type‐specific. LpMab‐21 combined with other anti‐hPDPN antibodies that recognize different epitopes may therefore be useful for determining the physiological function of sialylated hPDPN.
John Wiley & Sons
© 2016 The Authors. Cancer Medicine published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License(https://creativecommons.org/licenses/by/4.0/), which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
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